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Volumn 91, Issue 3, 2006, Pages 927-937

Reconstruction of a kinetic model of the chromatophore vesicles from Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C2; MEMBRANE PROTEIN; PROTON; UBIQUINONE;

EID: 33746715610     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.067561     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 4544227574 scopus 로고    scopus 로고
    • Toward large-scale modeling of the microbial cell for computer simulation
    • Ishii, N., M. Robert, Y. Nakayama, A. Kanai, and M. Tomita. 2004. Toward large-scale modeling of the microbial cell for computer simulation. J. Biotechnol. 113:281-294.
    • (2004) J. Biotechnol. , vol.113 , pp. 281-294
    • Ishii, N.1    Robert, M.2    Nakayama, Y.3    Kanai, A.4    Tomita, M.5
  • 2
    • 9544253891 scopus 로고    scopus 로고
    • Genome-scale models of microbial cells: Evaluating the consequences of constraints
    • Price, N. D., J. L. Reed, and B. O. Palsson. 2004. Genome-scale models of microbial cells: evaluating the consequences of constraints. Nat. Rev. Microbiol. 2:886-897.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 886-897
    • Price, N.D.1    Reed, J.L.2    Palsson, B.O.3
  • 3
    • 13444278821 scopus 로고    scopus 로고
    • Reconstruction of cellular signalling networks and analysis of their properties
    • Papin, J., T. Hunter, B. O. Palsson, and S. Subramanian. 2005. Reconstruction of cellular signalling networks and analysis of their properties. Nat. Rev. Mol. Cell Biol. 6:99-111.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 99-111
    • Papin, J.1    Hunter, T.2    Palsson, B.O.3    Subramanian, S.4
  • 4
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen, J. P., G. Feher, T. O. Yeates, H. Komiya, and D. C. Rees. 1987. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc. Natl. Acad. Sci. USA. 84:6162-6166.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 5
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 6
    • 0032568640 scopus 로고    scopus 로고
    • Architecture and mechanism of the light harvesting apparatus of purple bacteria
    • Hu, X., A. Damjanović, T. Ritz, and K. Schulten. 1998. Architecture and mechanism of the light harvesting apparatus of purple bacteria. Proc. Natl. Acad. Sci. USA. 95:5935-5941.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5935-5941
    • Hu, X.1    Damjanović, A.2    Ritz, T.3    Schulten, K.4
  • 7
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • Koepke, J., X. Hu, C. Muenke, K. Schulten, and H. Michel. 1996. The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure. 4:581-597.
    • (1996) Structure , vol.4 , pp. 581-597
    • Koepke, J.1    Hu, X.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 12
    • 0031920484 scopus 로고    scopus 로고
    • Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinones of various isoprenoid chain lengths incorporated in model bilayers
    • Marchal, D., W. Boireau, J. M. Laval, J. Moiroux, and C. Bourdillon. 1998. Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinones of various isoprenoid chain lengths incorporated in model bilayers. Biophys. J. 74:1937-1948.
    • (1998) Biophys. J. , vol.74 , pp. 1937-1948
    • Marchal, D.1    Boireau, W.2    Laval, J.M.3    Moiroux, J.4    Bourdillon, C.5
  • 14
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • Jungas, C., J.-L. Ranck, J.-L. Rigaud, P. Joliot, and A. Verméglio. 1999. Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides. EMBO J. 18:534-542.
    • (1999) EMBO J. , vol.18 , pp. 534-542
    • Jungas, C.1    Ranck, J.-L.2    Rigaud, J.-L.3    Joliot, P.4    Verméglio, A.5
  • 15
    • 0942287196 scopus 로고    scopus 로고
    • Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides
    • Scheuring, S., F. Francia, J. Busselez, B. A. Melandri, J.-L. Rigaud, and D. Lévy. 2004. Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides. J. Biol. Chem. 279:3620-3626.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.A.4    Rigaud, J.-L.5    Lévy, D.6
  • 17
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX
    • Siebert, C. A., P. Qian, D. Fotiadis, A. Engel, C. N. Hunter, and P. A. Bullough. 2004. Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX. EMBO J. 23:690-700.
    • (2004) EMBO J. , vol.23 , pp. 690-700
    • Siebert, C.A.1    Qian, P.2    Fotiadis, D.3    Engel, A.4    Hunter, C.N.5    Bullough, P.A.6
  • 20
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: Dynamics of regulatory and signaling pathways in the cell
    • Tyson, J. L., K. C. Chen, and B. Novak. 2003. Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell. Curr. Opin. Cell Biol. 15:221-231.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 221-231
    • Tyson, J.L.1    Chen, K.C.2    Novak, B.3
  • 22
    • 3042767574 scopus 로고    scopus 로고
    • The Q-cycle - A personal perspective
    • Crofts, A. R. 2004. The Q-cycle - a personal perspective. Photosynth. Res. 80:223-243.
    • (2004) Photosynth. Res. , vol.80 , pp. 223-243
    • Crofts, A.R.1
  • 23
    • 0033552946 scopus 로고    scopus 로고
    • Robustness in bacterial chemotaxis
    • Alon, U., M. G. Surette, N. Barkai, and S. Leibler. 1999. Robustness in bacterial chemotaxis. Nature. 397:168-171.
    • (1999) Nature , vol.397 , pp. 168-171
    • Alon, U.1    Surette, M.G.2    Barkai, N.3    Leibler, S.4
  • 25
    • 0000027407 scopus 로고
    • The size of the photosynthetic unit in purple bacteria
    • Francke, C., and J. Amesz. 1995. The size of the photosynthetic unit in purple bacteria. Photosynth. Res. 46:347-352.
    • (1995) Photosynth. Res. , vol.46 , pp. 347-352
    • Francke, C.1    Amesz, J.2
  • 27
    • 0033593069 scopus 로고    scopus 로고
    • Unbinding of oxidized Cytochrome c from photosynthetic reaction center of Rhodobacter sphaeroides is the bottleneck of fast turnover
    • Gerencsér, L., G. Laczkó, and P. Maróti. 1999. Unbinding of oxidized Cytochrome c from photosynthetic reaction center of Rhodobacter sphaeroides is the bottleneck of fast turnover. Biochemistry. 38:16866-16875.
    • (1999) Biochemistry , vol.38 , pp. 16866-16875
    • Gerencsér, L.1    Laczkó, G.2    Maróti, P.3
  • 28
    • 0002733503 scopus 로고
    • Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: Sequence analysis and preliminary characterization
    • Paddock, M. L., S. H. Rongey, E. C. Abresch, G. Feher, and M. Y. Okamura. 1988. Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: sequence analysis and preliminary characterization. Photosynth. Res. 17:75-96.
    • (1988) Photosynth. Res. , vol.17 , pp. 75-96
    • Paddock, M.L.1    Rongey, S.H.2    Abresch, E.C.3    Feher, G.4    Okamura, M.Y.5
  • 29
    • 0344825194 scopus 로고    scopus 로고
    • b site of reaction centers from the purple bacteria Rhodobacter sphaeroides reconstituted in liposomes
    • b site of reaction centers from the purple bacteria Rhodobacter sphaeroides reconstituted in liposomes. Eur. J. Biochem. 270:4595-4605.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4595-4605
    • Milano, F.1    Agostiano, A.2    Mavelli, F.3    Trotta, M.4
  • 31
    • 0011876383 scopus 로고
    • Energetic aspects of photophosphorylation capacity and reaction center content of Rhodopseudomonas capsulata, grown in a turbidostat under different irradiances
    • Reidl, H., J. R. Golecki, and G. Drews. 1983. Energetic aspects of photophosphorylation capacity and reaction center content of Rhodopseudomonas capsulata, grown in a turbidostat under different irradiances. Biochim. Biophys. Acta. 725:455-463.
    • (1983) Biochim. Biophys. Acta , vol.725 , pp. 455-463
    • Reidl, H.1    Golecki, J.R.2    Drews, G.3
  • 32
    • 9144264281 scopus 로고    scopus 로고
    • Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum
    • Scheuring, S., J.-L. Rigaud, and J. N. Sturgis. 2004. Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum. EMBO J. 23:4127-4133.
    • (2004) EMBO J. , vol.23 , pp. 4127-4133
    • Scheuring, S.1    Rigaud, J.-L.2    Sturgis, J.N.3
  • 33
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of an intersubunit disulfide bond between Cytochrome b and the iron-sulfur protein
    • 1 complex by the formation of an intersubunit disulfide bond between Cytochrome b and the iron-sulfur protein. J. Biol. Chem. 275:38597-38604.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.-A.3
  • 36
    • 0026035079 scopus 로고
    • ATP synthesis in chromatophores driven by artificially induced ion gradients
    • Turina, P., B. A. Melandri, and P. Gräber. 1991. ATP synthesis in chromatophores driven by artificially induced ion gradients. Eur. J. Biochem. 196:225-229.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 225-229
    • Turina, P.1    Melandri, B.A.2    Gräber, P.3
  • 42
    • 2942675081 scopus 로고    scopus 로고
    • The proton-driven rotor of ATP synthase: Ohmic conductance (10 fS), and absence of voltage gating
    • Feniouk, B. A., M. A. Kozlova, D. A. Knorre, D. A. Cherepanov, A. Y. Mulkidjanian, and W. Junge. 2004. The proton-driven rotor of ATP synthase: Ohmic conductance (10 fS), and absence of voltage gating. Biophys. J. 86:4094-4109.
    • (2004) Biophys. J. , vol.86 , pp. 4094-4109
    • Feniouk, B.A.1    Kozlova, M.A.2    Knorre, D.A.3    Cherepanov, D.A.4    Mulkidjanian, A.Y.5    Junge, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.